5xbj

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'''Unreleased structure'''
 
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The entry 5xbj is ON HOLD
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==The structure of the flagellar hook junction protein HAP1 (FlgK) from Campylobacter jejuni==
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<StructureSection load='5xbj' size='340' side='right'caption='[[5xbj]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xbj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XBJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.448&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xbj OCA], [https://pdbe.org/5xbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xbj RCSB], [https://www.ebi.ac.uk/pdbsum/5xbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xbj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q0P8E9_CAMJE Q0P8E9_CAMJE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Evolution of a nano-machine consisting of multiple parts, each with a specific function, is a complex process. A change in one part should eventually result in changes in other parts, if the overall function is to be conserved. In bacterial flagella, the filament and the hook have distinct functions and their respective proteins, FliC and FlgE, have different three-dimensional structures. The filament functions as a helical propeller and the hook as a flexible universal joint. Two proteins, FlgK and FlgL, assure a smooth connectivity between the hook and the filament. Here we show that, in Campylobacter, the 3D structure of FlgK differs from that of its orthologs in Salmonella and Burkholderia, whose structures have previously been solved. Docking the model of the FlgK junction onto the structure of the Campylobacter hook provides some clues about its divergence. These data suggest how evolutionary pressure to adapt to structural constraints, due to the structure of Campylobacter hook, causes divergence of one element of a supra-molecular complex in order to maintain the function of the entire flagellar assembly.
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Authors:
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Structure of FlgK reveals the divergence of the bacterial Hook-Filament Junction of Campylobacter.,Bulieris PV, Shaikh NH, Freddolino PL, Samatey FA Sci Rep. 2017 Nov 16;7(1):15743. doi: 10.1038/s41598-017-15837-0. PMID:29147015<ref>PMID:29147015</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5xbj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Campylobacter jejuni]]
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[[Category: Large Structures]]
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[[Category: Samatey FA]]

Current revision

The structure of the flagellar hook junction protein HAP1 (FlgK) from Campylobacter jejuni

PDB ID 5xbj

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